ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9Y275


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TN13B_HUMAN
Primary accession number Q9Y275
Secondary accession numbers None
Integrated into Swiss-Prot on February 21, 2001
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 100)
Name and origin of the protein
Protein name Tumor necrosis factor ligand superfamily member 13B
Synonyms TNF- and APOL-related leukocyte expressed ligand 1
TALL-1
B lymphocyte stimulator
BLyS
B cell-activating factor
BAFF
Dendritic cell-derived TNF-like molecule
CD257 antigen
Contains Tumor necrosis factor ligand superfamily member 13b, membrane form
Tumor necrosis factor ligand superfamily member 13b, soluble form
Gene name
Name: TNFSF13B
Synonyms: BAFF, BLYS, TALL1, TNFSF20, ZTNF4
ORFNames: UNQ401/PRO738
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10331498 [NCBI, ExPASy, EBI, Israel, Japan]
Shu H.-B., Hu W.-H., Johnson H.;
"TALL-1 is a novel member of the TNF family that is down-regulated by mitogens.";
J. Leukoc. Biol. 65:680-683(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 134-148.
DOI=10.1084/jem.189.11.1747; PubMed=10359578 [NCBI, ExPASy, EBI, Israel, Japan]
Schneider P., MacKay F., Steiner V., Hofmann K., Bodmer J.-L., Holler N., Ambrose C., Lawton P., Bixler S., Acha-Orbea H., Valmori D., Romero P., Werner-Favre C., Zubler R.H., Browning J.L., Tschopp J.;
"BAFF, a novel ligand of the tumor necrosis factor family, stimulates B cell growth.";
J. Exp. Med. 189:1747-1756(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Monocyte, and Neutrophil;
DOI=10.1126/science.285.5425.260; PubMed=10398604 [NCBI, ExPASy, EBI, Israel, Japan]
Moore P.A., Belvedere O., Orr A., Pieri K., LaFleur D.W., Feng P., Soppet D., Charters M., Gentz R., Parmelee D., Li Y., Galperina O., Giri J., Roschke V., Nardelli B., Carrell J., Sosnovtseva S., Greenfield W., Ruben S.M., Olsen H.S., Fikes J., Hilbert D.M.;
"BLyS: member of the tumor necrosis factor family and B lymphocyte stimulator.";
Science 285:260-263(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Farrah T., Gross J., Piddington C., O'Hara P.;
"Homo sapiens homolog of tumor necrosis factor.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Dendritic cell;
Zhang W., Wan T., Yu Y., Cao X.;
"A novel dendritic cell-derived TNF-like molecule.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan]
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135, AND VARIANT THR-105.
Kawasaki A., Tsuchiya N., Fukazawa T., Hashimoto H., Tokunaga K.;
"New polymorphisms of human BLyS gene.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION.
DOI=10.1038/79802; PubMed=10973284 [NCBI, ExPASy, EBI, Israel, Japan]
Yu G., Boone T., Delaney J., Hawkins N., Kelley M.J., Ramakrishnan M., McCabe S., Qiu W.R., Kornuc M., Xia X.-Z., Guo J., Stolina M., Boyle W.J., Sarosi I., Hsu H., Senaldi G., Theill L.E.;
"APRIL and TALL-I and receptors BCMA and TACI: system for regulating humoral immunity.";
Nat. Immunol. 1:252-256(2000).
[10]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 142-285.
DOI=10.1016/S0092-8674(02)00631-1; PubMed=11853672 [NCBI, ExPASy, EBI, Israel, Japan]
Liu Y., Xu L., Opalka N., Kappler J., Shu H.-B., Zhang G.;
"Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands.";
Cell 108:383-394(2002).
[11]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 136-285.
DOI=10.1006/jmbi.2001.5296; PubMed=11827482 [NCBI, ExPASy, EBI, Israel, Japan]
Karpusas M., Cachero T.G., Qian F., Boriack-Sjodin A., Mullen C., Strauch K., Hsu Y.-M., Kalled S.L.;
"Crystal structure of extracellular human BAFF, a TNF family member that stimulates B lymphocytes.";
J. Mol. Biol. 315:1145-1154(2002).
[12]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 134-285.
DOI=10.1038/nsb769; PubMed=11862220 [NCBI, ExPASy, EBI, Israel, Japan]
Oren D.A., Li Y., Volovik Y., Morris T.S., Dharia C., Das K., Galperina O., Gentz R., Arnold E.;
"Structural basis of BLyS receptor recognition.";
Nat. Struct. Biol. 9:288-292(2002).
Comments
  • FUNCTION: Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response.
  • SUBUNIT: Homotrimer.
  • INTERACTION:
    O14836:TNFRSF13B; NbExp=4; IntAct=EBI-519169, EBI-519160;
    Q02223:TNFRSF17; NbExp=1; IntAct=EBI-519169, EBI-519945;
  • SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.
  • SUBCELLULAR LOCATION: Tumor necrosis factor ligand superfamily member 13b, soluble form: Secreted.
  • TISSUE SPECIFICITY: Abundantly expressed in peripheral blood Leukocytes and is specifically expressed in monocytes and macrophages. Also found in the spleen, lymph node, bone marrow, T-cells and dendritic cells. A lower expression seen in placenta, heart, lung, fetal liver, thymus, and pancreas.
  • INDUCTION: Up-regulated by exposure to interferon-gamma. Down-regulated by phorbol myristate acetate/ionomycin treatment.
  • PTM: The soluble form derives from the membrane form by proteolytic processing.
  • PTM: N-glycosylated.
  • SIMILARITY: Belongs to the tumor necrosis factor family.
  • WEB RESOURCE: Name=Protein Spotlight; Note=Proteic grace - Issue 77 of December 2006; URL="http://www.expasy.org/spotlight/back_issues/sptlt077.shtml";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF136293; AAD29421.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF116456; AAD25356.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF132600; AAD21092.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF186114; AAF01432.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134715; AAF60219.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB073225; BAB90856.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358881; AAQ89240.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020674; AAH20674.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00031802; -.
RefSeq NP_006564.1; -.
UniGene Hs.525157
3D structure databases
PDB
1JH5; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=142-285.[ExPASy / RCSB / EBI]
1KD7; X-ray; 2.80 A; A/B/C/K/L/M=136-285.[ExPASy / RCSB / EBI]
1KXG; X-ray; 2.00 A; A/B/C/D/E/F=134-285.[ExPASy / RCSB / EBI]
1OQD; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J=142-285.[ExPASy / RCSB / EBI]
1OQE; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J=142-285.[ExPASy / RCSB / EBI]
1OSG; X-ray; 3.00 A; A/B/C/D/E/F=82-285.[ExPASy / RCSB / EBI]
1OTZ; X-ray; 3.30 A; 0/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d/e/f/g/h/i/j/k/l/m/n/o/p/q/r/s/t/u/v/w/x=138-285.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1JH5; -.
1KD7; -.
1KXG; -.
1OQD; -.
1OQE; -.
1OSG; -.
1OTZ; -.
ModBase Q9Y275.
Protein-protein interaction databases
IntAct Q9Y275; 2.
Organism-specific databases
GeneCards GC13P107719; -.
H-InvDB HIX0011450; -.
HGNC HGNC:11929; TNFSF13B.
GenAtlas TNFSF13B.
HPA CAB009188; -.
MIM 603969; gene. [NCBI / EBI]
PharmGKB PA434; -.
Gene expression databases
ArrayExpress Q9Y275; -.
Bgee Q9Y275; -.
CleanEx HS_TNFSF13B; -.
GermOnline ENSG00000102524; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from electronic annotation from UniProtKB-KW).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0005125; Molecular function: cytokine activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005164; Molecular function: tumor necrosis factor receptor binding (inferred from electronic annotation from InterPro).
GO:0008283; Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR006052; TNF_family.
IPR008983; Tumour_necrosis_fac-like.
Graphical view of domain structure.
Gene3D G3DSA:2.60.120.40; Tumour_necrosis_fac-like; 1.
Pfam PF00229; TNF; 1.
Pfam graphical view of domain structure.
SMART SM00207; TNF; 1.
SMART graphical view of domain structure.
PROSITE PS00251; TNF_1; FALSE_NEG.
PS50049; TNF_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q9Y275; -.
Genome annotation databases
Ensembl ENSG00000102524; Homo sapiens. [Contig view]
GeneID 10673; -.
KEGG hsa:10673; -.
Phylogenomic databases
HOGENOM Q9Y275; -.
HOVERGEN Q9Y275; -.
OMA Q9Y275; LALLSCC.
Other
NextBio 40587; -.
SOURCE TNFSF13B; Homo sapiens.
ProtoNet Q9Y275.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell membrane; Cleavage on pair of basic residues; Cytokine; Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane; Polymorphism; Secreted; Signal-anchor; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   285  285     Tumor necrosis factor ligand superfamily member 13b, membrane form. PRO_0000034528
CHAIN   134   285  152     Tumor necrosis factor ligand superfamily member 13b, soluble form. PRO_0000034529
TOPO_DOM   1    46  46     Cytoplasmic (Potential). 
TRANSMEM   47    67  21     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   68   285  218     Extracellular (Potential). 
SITE   133   134  2     Cleavage. 
CARBOHYD   124   124        N-linked (GlcNAc...). 
CARBOHYD   242   242        N-linked (GlcNAc...) (high mannose). 
DISULFID   232   245         
VARIANT   105   105  1     A -> T. VAR_013483 
STRAND   146   151  6      
STRAND   158   160  3      
STRAND   163   165  3      
STRAND   168   181  14      
STRAND   184   187  4      
STRAND   191   201  11      
STRAND   205   215  11      
STRAND   225   235  11      
STRAND   238   240  3      
STRAND   243   253  11      
STRAND   258   265  8      
TURN   274   276  3      
STRAND   277   283  7      
Sequence information
Length: 285 AA [This is the length of the unprocessed precursor] Molecular weight: 31223 Da [This is the MW of the unprocessed precursor] CRC64: 48ED0D7AB38C8867 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDDSTEREQS RLTSCLKKRE EMKLKECVSI LPRKESPSVR SSKDGKLLAA TLLLALLSCC 

        70         80         90        100        110        120 
LTVVSFYQVA ALQGDLASLR AELQGHHAEK LPAGAGAPKA GLEEAPAVTA GLKIFEPPAP 

       130        140        150        160        170        180 
GEGNSSQNSR NKRAVQGPEE TVTQDCLQLI ADSETPTIQK GSYTFVPWLL SFKRGSALEE 

       190        200        210        220        230        240 
KENKILVKET GYFFIYGQVL YTDKTYAMGH LIQRKKVHVF GDELSLVTLF RCIQNMPETL 

       250        260        270        280 
PNNSCYSAGI AKLEEGDELQ LAIPRENAQI SLDGDVTFFG ALKLL 

Q9Y275 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!